Search results for "Prions"

showing 10 items of 23 documents

Gastric α-synuclein immunoreactive inclusions in Meissner's and Auerbach's plexuses in cases staged for Parkinson's disease-related brain pathology

2005

The progressive degenerative process associated with sporadic Parkinson's disease (sPD) is characterized by formation of alpha-synuclein-containing inclusion bodies in a few types of projection neurons in both the enteric and central nervous systems (ENS and CNS). In the brain, the process apparently begins in the brainstem (dorsal motor nucleus of the vagal nerve) and advances through susceptible regions of the basal mid-and forebrain until it reaches the cerebral cortex. Anatomically, all of the vulnerable brain regions are closely interconnected. Whether the pathological process begins in the brain or elsewhere in the nervous system, however, is still unknown. We therefore used immunocyt…

MaleNervous systemProtein FoldingPathologymedicine.medical_specialtyPrionsModels NeurologicalCentral nervous systemMyenteric PlexusBiologyAxonal TransportCentral nervous system diseaseNeural PathwaysDisease Transmission InfectiousmedicineHumansAgedAged 80 and overInclusion BodiesNeuronsGeneral NeuroscienceBrainParkinson DiseaseVagus NerveSubmucous PlexusMiddle Agedmedicine.diseasemedicine.anatomical_structureDorsal motor nucleusGastric MucosaCerebral cortexForebrainalpha-SynucleinFemaleEnteric nervous systemBrainstemNerve NetNeuroscienceNeuroscience Letters
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Quantitative and integrative proteome analysis of peripheral nerve myelin identifies novel myelin proteins and candidate neuropathy loci

2011

Peripheral nerve myelin facilitates rapid impulse conduction and normal motor and sensory functions. Many aspects of myelin biogenesis, glia–axonal interactions, and nerve homeostasis are poorly understood at the molecular level. We therefore hypothesized that only a fraction of all relevant myelin proteins has been identified so far. Combining gel-based and gel-free proteomic approaches, we identified 545 proteins in purified mouse sciatic nerve myelin, including 36 previously known myelin constituents. By mass spectrometric quantification, the predominant P0, periaxin, and myelin basic protein constitute 21, 16, and 8% of the total myelin protein, respectively, suggesting that their relat…

MaleProteomicsCandidate geneProteomePrions10208 Institute of Neuropathology610 Medicine & healthHereditary neuralgic amyotrophyTetraspanin 24BiologySeptinTranscriptomeMice03 medical and health sciencesMyelin0302 clinical medicinemedicineAnimalsElectrophoresis Gel Two-DimensionalRNA MessengerMyelin Sheath030304 developmental biologyMice KnockoutGenetics0303 health sciencesGeneral NeuroscienceComputational BiologyMembrane Proteins2800 General NeuroscienceArticlesmedicine.diseaseSciatic NerveCell biologyMyelin basic proteinMice Inbred C57BLMolecular Weightmedicine.anatomical_structureAnimals Newbornnervous systemSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProteomebiology.protein570 Life sciences; biologyChemokinesMyelin ProteinsSeptins030217 neurology & neurosurgeryBiogenesisDemyelinating Diseases
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Prions, mad cow disease, and preventive measures: a critical appraisal

2003

In 1996 the first key epidemiological study on bovine spongiform encephalitis (BSE) appeared in the renowned journal Nature [1]. In that article it was estimated that by the year 1996, some 750,000 cows with BSE had entered the food chain in Great Britain. Accordingly, millions of people in GB must have consumed contaminated meat. That same year the first report on a new form of Creutzfeldt-Jakob disease [variant (v) CJD] manifesting in young patients appeared [26]. A connection between this disease and BSE was assumed. In view of the suspicion that the use of meat and bone meal (MBM) had led to the outbreak of BSE, feeding with MBM was banned in the year 1988. The number of new BSE infecti…

Microbiology (medical)Veterinary medicinemedicine.medical_specialtyPrPSc ProteinsPrionsanimal diseasesBovine spongiform encephalopathyImmunologySheep DiseasesCullingDiseaseCreutzfeldt-Jakob SyndromePrion DiseasesEnvironmental healthmental disordersEpidemiologymedicineAnimalsHumansImmunology and AllergyPrPC ProteinsSheepKurubusiness.industryIncidencefood and beveragesOutbreakGeneral MedicineCreutzfeldt-Jakob Syndromemedicine.diseaseMeat and bone mealnervous system diseasesEncephalopathy Bovine SpongiformKuruCattlebusinessScrapieMedical Microbiology and Immunology
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Pertuzumab monotherapy after trastuzumab-based treatment and subsequent reintroduction of trastuzumab: activity and tolerability in patients with adv…

2012

Purpose The combination of pertuzumab and trastuzumab resulted in a clinical benefit rate (CBR) of 50% in patients with human epidermal growth factor receptor 2 (HER2) –positive breast cancer whose disease progressed during prior trastuzumab-based therapy. To define whether this previously observed encouraging activity was a result of the combination of pertuzumab and trastuzumab or of pertuzumab alone, we recruited a third cohort of patients who received pertuzumab without trastuzumab. We then investigated the impact of reintroducing trastuzumab to patients whose disease progressed on pertuzumab monotherapy. Patients and Methods Twenty-nine patients with HER2-positive breast cancer whose d…

OncologyCancer ResearchReceptor ErbB-2MESH: Risk AssessmentMESH: Dose-Response Relationship Drug0302 clinical medicineTrastuzumabAntineoplastic Combined Chemotherapy ProtocolsMedicineProspective StudiesProspective cohort studyskin and connective tissue diseasespertuzumab; trastuzumab; breast cancerMESH: Treatment OutcomeMESH: Aged0303 health sciencesMESH: Middle AgedMESH: ErythrocytesAge FactorsMESH: Maximum Tolerated DoseMESH: Neoplasm StagingMiddle AgedPrognosis3. Good healthtrastuzumabMESH: Antineoplastic Combined Chemotherapy ProtocolsTreatment OutcomeOncologyTolerabilityMESH: Receptor erbB-2030220 oncology & carcinogenesisMESH: Survival AnalysisDisease Progression[SDV.IMM]Life Sciences [q-bio]/ImmunologyMESH: Disease ProgressionFemalePertuzumabmedicine.drugAdultmedicine.medical_specialty[SDV.IMM] Life Sciences [q-bio]/ImmunologyMaximum Tolerated DoseMESH: Blood TransfusionBreast NeoplasmsMESH: Drug Administration ScheduleAntibodies Monoclonal HumanizedLoading doseMESH: Cell SeparationRisk AssessmentMESH: PrognosisDisease-Free SurvivalDrug Administration Schedule03 medical and health sciencesbreast cancerBreast cancerMESH: PrionspertuzumabInternal medicineHumansMESH: Patient SelectionNeoplasm InvasivenessneoplasmsSurvival analysis030304 developmental biologyAgedNeoplasm StagingMESH: Age FactorsMESH: HumansDose-Response Relationship Drugbusiness.industryPatient SelectionMESH: AdultMESH: Neoplasm InvasivenessMESH: Creutzfeldt-Jakob SyndromeTrastuzumabmedicine.diseaseSurvival AnalysisMESH: Prospective StudiesMESH: Antibodies Monoclonal HumanizedMESH: Disease-Free SurvivalbusinessMESH: FemaleProgressive diseaseMESH: Breast NeoplasmsJournal of clinical oncology : official journal of the American Society of Clinical Oncology
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Cytoprotective effect of NMDA receptor antagonists on prion protein (PrionSc)-induced toxicity in rat cortical cell cultures

1993

Rat cortical cells were incubated with the Scrapie prion protein, PrionSc. At concentrations of 3 ng/ml of PrionSc and higher, the viability of the cells decreased significantly after a 12-h incubation period. Simultaneously, the degree of DNA fragmentation increased. In control experiments with antibodies against PrionSc, PrionSc lost its deleterious effect on neurons. PrionSc did not affect the viability of astrocytes. Drugs known to block NMDA receptor channels, such as memantine (1-amino-3,5-dimethyl-adamantane) (Mem), its analogue 1-N-methylamino-3,5-dimethyl-adamantane as well as (+)-5-methyl-10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5,10-imine maleate (MK-801) prevented the effect of …

PrPSc ProteinsCell SurvivalPrionsNerve Tissue ProteinsScrapiePharmacologyReceptors N-Methyl-D-AspartateIncubation periodNeuroblastomaTumor Cells CulturedmedicineAnimalsRats WistarCells CulturedCerebral CortexNeuronsPharmacologybiologyMemantineCalcium Channel BlockersIn vitroRatsAstrocytesLiposomesToxicityImmunologybiology.proteinDNA fragmentationNMDA receptorAntibodymedicine.drugEuropean Journal of Pharmacology: Molecular Pharmacology
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De Novo prion aggregates trigger autophagy in skeletal muscle

2014

ABSTRACT In certain sporadic, familial, and infectious prion diseases, the prion protein misfolds and aggregates in skeletal muscle in addition to the brain and spinal cord. In myocytes, prion aggregates accumulate intracellularly, yet little is known about clearance pathways. Here we investigated the clearance of prion aggregates in muscle of transgenic mice that develop prion disease de novo . In addition to neurodegeneration, aged mice developed a degenerative myopathy, with scattered myocytes containing ubiquitinated, intracellular prion inclusions that were adjacent to myocytes lacking inclusions. Myocytes also showed elevated levels of the endoplasmic reticulum chaperone Grp78/BiP, su…

PrionsAutophagosome maturationanimal diseasesBlotting WesternImmunologyMice TransgenicBiologyProtein degradationPolymerase Chain ReactionMedical and Health SciencesMicrobiologyTransgenicPrion DiseasesMiceVirologyAutophagymedicineAnimalsMyocyteMuscle SkeletalEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsDNA PrimersMuscle CellsAgricultural and Veterinary SciencesBlottingEndoplasmic reticulumNeurodegenerationAutophagySkeletal muscleSkeletalBiological Sciencesmedicine.diseaseImmunohistochemistryMolecular biologynervous system diseasesmedicine.anatomical_structureInsect ScienceChaperone (protein)biology.proteinMuscleWestern
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Interaction of 68–kDa TAR RNA-binding protein and other cellular proteins with rpion protein-RNA stem-loop

1995

The RNA stem-loop structure of the trans-activating region TAR sequence of human immunodeficiency virus-1 mRNA is the binding site for a number of host cell proteins. A virtually identical set of proteins from HeLa nuclear extracts was found to bind to the predicted RNA hairpin element of prion protein (PrP) mRNA, as demonstrated in UV cross-linking/RNase protection and Northwestern assays. We show that the cellular TAR loop-binding protein, p68, is among those proteins which associate with PrP RNA. Competition experiments with various TAR RNA mutants revealed that binding of partially purified p68 to PrP RNA stem-loop occurs sequence-specifically. The 100-kDa 2-5A synthetase which is invol…

PrionsBlotting WesternMolecular Sequence DataRNA-dependent RNA polymeraseReceptors Cell SurfaceRNA-binding proteinBiologyBinding CompetitiveCellular and Molecular NeuroscienceVirology2'5'-Oligoadenylate SynthetaseHumansLymphocytesHIV Long Terminal RepeatBase SequenceRNA-Binding ProteinsRNABlotting NorthernNon-coding RNAMolecular biologyRNA silencingNeurologyMutagenesisRNA editingeIF4ANucleic Acid ConformationNeurology (clinical)Small nuclear RNAHeLa CellsJournal of Neurovirology
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Effect of flupirtine on Bcl-2 and glutathione level in neuronal cells treated in vitro with the prion protein fragment (PrP106-126).

1997

Flupirtine, trade name Katadolon, is a centrally acting nonopioid analgesic that has recently been found to display cytoprotective activity in vitro and in vivo on neurons induced to undergo apoptosis. This report shows that the PrP106-126 fragment of the prion protein, which is the likely etiological agent for a series of encephalopathies, is toxic to cortical neurons in vitro. Simultaneously, PrP106-126 influences the molecular GSH content and the bcl-2 expression in neurons. Significant toxicity (32% reduction in cell viability) was observed at a concentration of 50 microM of the peptide after 9 days of incubation, while at higher concentrations toxicity increased to 70%. Neurotoxicity w…

PrionsMolecular Sequence DataAminopyridinesApoptosisPharmacologyBiologychemistry.chemical_compoundDevelopmental NeurosciencemedicineAnimalsAmino Acid SequenceRats WistarCytotoxicityCells CulturedNeuronsNeurotoxicityGlutathioneAnalgesics Non-Narcoticmedicine.diseaseGlutathioneIn vitroPeptide FragmentsGenes bcl-2RatsOxidative StressNeuroprotective AgentsNeurologychemistryGene Expression RegulationProto-Oncogene Proteins c-bcl-2ApoptosisCell cultureImmunologyToxicityFlupirtineOxidation-Reductionmedicine.drugExperimental neurology
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Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

2009

Abstract Both the cellular prion protein (PrPc) and the amyloid precursor protein (APP) are physiologically subjected to complex proteolytic processing events. While for APP the proteinases involved – alpha-, beta- and gamma-secretase – have been identified in vitro and in vivo, the cleavage of PrPc by now has been linked only to the shedding activity of the metalloproteinase ADAM10 and/or ADAM17 in cell culture. Here we show that neuronal overexpression of the alpha-secretase ADAM10 in mice reduces all PrPc species detected in the brain instead of leading to enhanced amounts of specific cleavage products of PrPc. Additionally, the incubation time of mice after scrapie infection is signific…

Prionsanimal diseasesADAM10Molecular Sequence DataPrion diseaseScrapieMice Transgeniclcsh:RC321-571ADAM10 ProteinMiceIn vivomental disordersNeurotoxicitymedicineAmyloid precursor proteinAnimalsHumansGliosisAmino Acid Sequencealpha-Secretaselcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySheddingMetalloproteinasebiologyChemistryBrainMembrane ProteinsMolecular biologyIn vitronervous system diseasesMice Inbred C57BLADAM ProteinsNeurologyAlpha secretaseGliosisbiology.proteinCattlemedicine.symptomAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalScrapieNeurobiology of disease
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Quantitative Analysis of Prion-Protein Degradation by Constitutive and Immuno-20S Proteasomes Indicates Differences Correlated with Disease Susceptib…

2004

Abstract The main part of cytosolic protein degradation depends on the ubiquitin-proteasome system. Proteasomes degrade their substrates into small peptide fragments, some of which are translocated into the endoplasmatic reticulum and loaded onto MHC class I molecules, which are then transported to the cell surface for inspection by CTL. A reliable prediction of proteasomal cleavages in a given protein for the identification of CTL epitopes would benefit immensely from additional cleavage data for the training of prediction algorithms. To increase the knowledge about proteasomal specificity and to gain more insight into the relation of proteasomal activity and susceptibility to prion diseas…

Proteasome Endopeptidase ComplexPrionsMolecular Sequence DataImmunologyCellProtein degradationPeptide MappingMultienzyme ComplexesMHC class ImedicineAnimalsHumansImmunology and AllergyAmino Acid SequencePeptide sequenceAllelesCell Line TransformedSheepbiologyHydrolysisMolecular biologyPeptide FragmentsRecombinant ProteinsCell biologyCysteine EndopeptidasesKineticsCytosolCTL*medicine.anatomical_structureProteasomeCell culturebiology.proteinDisease SusceptibilityThe Journal of Immunology
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